Study of protein-CdTe quantum dot interactions.

This report presents a systematic study of the interaction mechanism between CdTe quantum dots (QDs) and three typical serum proteins [glucose oxidase (GOD), hemoglobin (Hb) and cytochrome c (Cyt C)] possessing different isoelectric points. The interactions were investigated through two approaches,...

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Main Author: Wang, Zheng.
Other Authors: Li Changming
Format: Final Year Project
Language:English
Published: 2009
Subjects:
Online Access:http://hdl.handle.net/10356/16382
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-163822023-03-03T15:39:12Z Study of protein-CdTe quantum dot interactions. Wang, Zheng. Li Changming School of Chemical and Biomedical Engineering DRNTU::Engineering::Chemical engineering::Biochemical engineering This report presents a systematic study of the interaction mechanism between CdTe quantum dots (QDs) and three typical serum proteins [glucose oxidase (GOD), hemoglobin (Hb) and cytochrome c (Cyt C)] possessing different isoelectric points. The interactions were investigated through two approaches, surface–attached approach and solution–phase approach, using techniques including surface plasmon resonance, atomic force microscopy, hydrodynamic size and zeta potential measurements, and photoluminescence spectrometry. Different binding behaviors of the three proteins and agglomeration of Hb-QD complex can be observed in the experiment results. Electrostatic attraction is proved to be the dominant interaction force of protein-QD associations. Based on the results, surface charge distribution and relative size of the proteins are proposed to be the two main factors determining the protein-QD interactions. This mechanism may also be extended to explain and predict the interaction of proteins and other nanoparticles with electrostatic attraction as the major binding force. Bachelor of Engineering (Chemical and Biomolecular Engineering) 2009-05-26T01:53:58Z 2009-05-26T01:53:58Z 2009 2009 Final Year Project (FYP) http://hdl.handle.net/10356/16382 en Nanyang Technological University 68 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Engineering::Chemical engineering::Biochemical engineering
spellingShingle DRNTU::Engineering::Chemical engineering::Biochemical engineering
Wang, Zheng.
Study of protein-CdTe quantum dot interactions.
description This report presents a systematic study of the interaction mechanism between CdTe quantum dots (QDs) and three typical serum proteins [glucose oxidase (GOD), hemoglobin (Hb) and cytochrome c (Cyt C)] possessing different isoelectric points. The interactions were investigated through two approaches, surface–attached approach and solution–phase approach, using techniques including surface plasmon resonance, atomic force microscopy, hydrodynamic size and zeta potential measurements, and photoluminescence spectrometry. Different binding behaviors of the three proteins and agglomeration of Hb-QD complex can be observed in the experiment results. Electrostatic attraction is proved to be the dominant interaction force of protein-QD associations. Based on the results, surface charge distribution and relative size of the proteins are proposed to be the two main factors determining the protein-QD interactions. This mechanism may also be extended to explain and predict the interaction of proteins and other nanoparticles with electrostatic attraction as the major binding force.
author2 Li Changming
author_facet Li Changming
Wang, Zheng.
format Final Year Project
author Wang, Zheng.
author_sort Wang, Zheng.
title Study of protein-CdTe quantum dot interactions.
title_short Study of protein-CdTe quantum dot interactions.
title_full Study of protein-CdTe quantum dot interactions.
title_fullStr Study of protein-CdTe quantum dot interactions.
title_full_unstemmed Study of protein-CdTe quantum dot interactions.
title_sort study of protein-cdte quantum dot interactions.
publishDate 2009
url http://hdl.handle.net/10356/16382
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